ID   TAL_VIBPA               Reviewed;         316 AA.
AC   Q87GY5;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00492};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00492}; OrderedLocusNames=VPA1180;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC         Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00492};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC       ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage):
CC       step 2/3. {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00492}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00492}.
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DR   EMBL; BA000032; BAC62523.1; -; Genomic_DNA.
DR   RefSeq; NP_800690.1; NC_004605.1.
DR   RefSeq; WP_005463537.1; NC_004605.1.
DR   AlphaFoldDB; Q87GY5; -.
DR   SMR; Q87GY5; -.
DR   STRING; 223926.28809548; -.
DR   EnsemblBacteria; BAC62523; BAC62523; BAC62523.
DR   GeneID; 1191876; -.
DR   KEGG; vpa:VPA1180; -.
DR   PATRIC; fig|223926.6.peg.4106; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_047470_0_1_6; -.
DR   OMA; KFGYKTL; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002493; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:transaldolase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00492; Transaldolase_1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004730; Transaldolase_1.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   PANTHER; PTHR10683:SF18; PTHR10683:SF18; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   TIGRFAMs; TIGR00874; talAB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..316
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173621"
FT   ACT_SITE        132
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   316 AA;  34806 MW;  3E6B53CB918026F9 CRC64;
     MSNKLEQLRK LTTVVADTGE IDAIKKYQPE DATTNPSLIL KAAQIAEYAP LIDASIEYAK
     AQSNDKAQQV QDTCDMLAVN IGKEILKTIP GRISTEVDAR LSYDMEGSVA KARQLVKMYN
     DAGITNDRIL IKLASTWEGI RAAEILEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG
     RIMDWYKAKE GRDFEASEDP GVLSVTKIYN YYKEYGYKTV VMGASFRNIG EILELAGCDR
     LTIAPALLAE LEAAEGEVVE KLVDSKGAAE RPAPMTHAEF LWEHNQDPMA VEKLAEGIRN
     FAVDQGKLEA MIEAKL